Detection of manganese peroxidase and other exoenzymes in four isolates of Geastrum (Geastrales) in pure culture

Knowledge regarding the enzymatic machinery of fungi is decisive to understand their ecological role. The species of the genus Geastrum are known to grow extremely slowly in pure culture, which makes it difficult to evaluate physiological parameters such as enzyme activity. Qualitative assays were p...

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Autores principales: Kuhar, F., Castiglia, V.C., Zamora, J.C.
Formato: JOUR
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_03257541_v48_n4_p274_Kuhar
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spelling todo:paper_03257541_v48_n4_p274_Kuhar2023-10-03T15:24:23Z Detection of manganese peroxidase and other exoenzymes in four isolates of Geastrum (Geastrales) in pure culture Kuhar, F. Castiglia, V.C. Zamora, J.C. Cellulase Laccase Lipase Litter degradation Xylanase amino acid amylase cellulase glycosidase laccase manganese peroxidase nitrophenol pectin polygalacturonase proton transporting adenosine triphosphate synthase ribosome DNA RNA polymerase II triacylglycerol lipase xenobiotic agent xylan 1,4 beta xylosidase xylan endo 1,3 beta xylosidase amylase carbon cellulase culture medium fungal protein laccase manganese peroxidase peroxidase polygalacturonase triacylglycerol lipase agar medium Article Cantharellales decolorization enzyme activity fungal cell culture Geastrum Geastrum argentinum Geastrum morganii Geastrum papinuttii Geastrum plicatum litter decomposition mycelium nonhuman Basidiomycetes comparative study culture medium enzymology growth, development and aging metabolism species difference Amylases Basidiomycota Carbon Cellulase Culture Media Fungal Proteins Laccase Lipase Peroxidases Polygalacturonase Species Specificity Knowledge regarding the enzymatic machinery of fungi is decisive to understand their ecological role. The species of the genus Geastrum are known to grow extremely slowly in pure culture, which makes it difficult to evaluate physiological parameters such as enzyme activity. Qualitative assays were performed on isolates of four species of this genus, showing evidence of laccase, cellulase, pectinase, amylase and lipase activity and suggesting that a wide range of carbon sources can be exploited by these species. For the first time in this genus, quantitative assays verified manganese peroxidase activity (up to 0.6 mU/g) in 30-day old cultures, as well as laccase, β-glycosidase and β-xylosidase activities. © 2016 Asociación Argentina de Microbiología Fil:Castiglia, V.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_03257541_v48_n4_p274_Kuhar
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Cellulase
Laccase
Lipase
Litter degradation
Xylanase
amino acid
amylase
cellulase
glycosidase
laccase
manganese peroxidase
nitrophenol
pectin
polygalacturonase
proton transporting adenosine triphosphate synthase
ribosome DNA
RNA polymerase II
triacylglycerol lipase
xenobiotic agent
xylan 1,4 beta xylosidase
xylan endo 1,3 beta xylosidase
amylase
carbon
cellulase
culture medium
fungal protein
laccase
manganese peroxidase
peroxidase
polygalacturonase
triacylglycerol lipase
agar medium
Article
Cantharellales
decolorization
enzyme activity
fungal cell culture
Geastrum
Geastrum argentinum
Geastrum morganii
Geastrum papinuttii
Geastrum plicatum
litter decomposition
mycelium
nonhuman
Basidiomycetes
comparative study
culture medium
enzymology
growth, development and aging
metabolism
species difference
Amylases
Basidiomycota
Carbon
Cellulase
Culture Media
Fungal Proteins
Laccase
Lipase
Peroxidases
Polygalacturonase
Species Specificity
spellingShingle Cellulase
Laccase
Lipase
Litter degradation
Xylanase
amino acid
amylase
cellulase
glycosidase
laccase
manganese peroxidase
nitrophenol
pectin
polygalacturonase
proton transporting adenosine triphosphate synthase
ribosome DNA
RNA polymerase II
triacylglycerol lipase
xenobiotic agent
xylan 1,4 beta xylosidase
xylan endo 1,3 beta xylosidase
amylase
carbon
cellulase
culture medium
fungal protein
laccase
manganese peroxidase
peroxidase
polygalacturonase
triacylglycerol lipase
agar medium
Article
Cantharellales
decolorization
enzyme activity
fungal cell culture
Geastrum
Geastrum argentinum
Geastrum morganii
Geastrum papinuttii
Geastrum plicatum
litter decomposition
mycelium
nonhuman
Basidiomycetes
comparative study
culture medium
enzymology
growth, development and aging
metabolism
species difference
Amylases
Basidiomycota
Carbon
Cellulase
Culture Media
Fungal Proteins
Laccase
Lipase
Peroxidases
Polygalacturonase
Species Specificity
Kuhar, F.
Castiglia, V.C.
Zamora, J.C.
Detection of manganese peroxidase and other exoenzymes in four isolates of Geastrum (Geastrales) in pure culture
topic_facet Cellulase
Laccase
Lipase
Litter degradation
Xylanase
amino acid
amylase
cellulase
glycosidase
laccase
manganese peroxidase
nitrophenol
pectin
polygalacturonase
proton transporting adenosine triphosphate synthase
ribosome DNA
RNA polymerase II
triacylglycerol lipase
xenobiotic agent
xylan 1,4 beta xylosidase
xylan endo 1,3 beta xylosidase
amylase
carbon
cellulase
culture medium
fungal protein
laccase
manganese peroxidase
peroxidase
polygalacturonase
triacylglycerol lipase
agar medium
Article
Cantharellales
decolorization
enzyme activity
fungal cell culture
Geastrum
Geastrum argentinum
Geastrum morganii
Geastrum papinuttii
Geastrum plicatum
litter decomposition
mycelium
nonhuman
Basidiomycetes
comparative study
culture medium
enzymology
growth, development and aging
metabolism
species difference
Amylases
Basidiomycota
Carbon
Cellulase
Culture Media
Fungal Proteins
Laccase
Lipase
Peroxidases
Polygalacturonase
Species Specificity
description Knowledge regarding the enzymatic machinery of fungi is decisive to understand their ecological role. The species of the genus Geastrum are known to grow extremely slowly in pure culture, which makes it difficult to evaluate physiological parameters such as enzyme activity. Qualitative assays were performed on isolates of four species of this genus, showing evidence of laccase, cellulase, pectinase, amylase and lipase activity and suggesting that a wide range of carbon sources can be exploited by these species. For the first time in this genus, quantitative assays verified manganese peroxidase activity (up to 0.6 mU/g) in 30-day old cultures, as well as laccase, β-glycosidase and β-xylosidase activities. © 2016 Asociación Argentina de Microbiología
format JOUR
author Kuhar, F.
Castiglia, V.C.
Zamora, J.C.
author_facet Kuhar, F.
Castiglia, V.C.
Zamora, J.C.
author_sort Kuhar, F.
title Detection of manganese peroxidase and other exoenzymes in four isolates of Geastrum (Geastrales) in pure culture
title_short Detection of manganese peroxidase and other exoenzymes in four isolates of Geastrum (Geastrales) in pure culture
title_full Detection of manganese peroxidase and other exoenzymes in four isolates of Geastrum (Geastrales) in pure culture
title_fullStr Detection of manganese peroxidase and other exoenzymes in four isolates of Geastrum (Geastrales) in pure culture
title_full_unstemmed Detection of manganese peroxidase and other exoenzymes in four isolates of Geastrum (Geastrales) in pure culture
title_sort detection of manganese peroxidase and other exoenzymes in four isolates of geastrum (geastrales) in pure culture
url http://hdl.handle.net/20.500.12110/paper_03257541_v48_n4_p274_Kuhar
work_keys_str_mv AT kuharf detectionofmanganeseperoxidaseandotherexoenzymesinfourisolatesofgeastrumgeastralesinpureculture
AT castigliavc detectionofmanganeseperoxidaseandotherexoenzymesinfourisolatesofgeastrumgeastralesinpureculture
AT zamorajc detectionofmanganeseperoxidaseandotherexoenzymesinfourisolatesofgeastrumgeastralesinpureculture
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